Reviewed, UniProtKB/Swiss-Prot P08514 (ITA2B_HUMAN)

Names and origin

Protein names

Recommended name:
    Integrin alpha-IIb
Alternative name(s):
    Platelet membrane glycoprotein IIb
    GPalpha IIb
      Short name=GPIIb
    CD_antigen=CD41
Cleaved into the following 3 chains:
    1- Recommended name:
            Integrin alpha-IIb heavy chain
    2- Recommended name:
            Integrin alpha-IIb light chain, form 1
    3- Recommended name:
            Integrin alpha-IIb light chain, form 2

Gene names

Name:	ITGA2B
Synonyms:	GP2B, ITGAB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1039 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.
Subunit structure	Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Ref.22
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.
Polymorphism	Position 874 is associated with platelet-specific alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).
Involvement in disease	Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:273800]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors. Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45
Sequence similarities	Belongs to the integrin alpha chain family. Contains 7 FG-GAP repeats.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal Transmembrane
Ligand	Calcium
Molecular function	Integrin Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integrin complex Inferred from electronic annotation. Source: InterPro platelet alpha granule membrane Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-702693,EBI-702693

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P08514-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P08514-2)

The sequence of this isoform differs from the canonical sequence as follows:
     948-981: Missing.

Isoform 3 (identifier: P08514-3)

The sequence of this isoform differs from the canonical sequence as follows:
     910-1039: SCDSAPCTVV...PLEEDDEEGE → VSRLSGLWPG...ATLGPWEHFK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Ref.11 Ref.12

Chain

32 – 1039

1008

Integrin alpha-IIb

PRO_0000016275

Chain

32 – 887

856

Integrin alpha-IIb heavy chain

PRO_0000016276

Chain

891 – 1039

149

Integrin alpha-IIb light chain, form 1

PRO_0000292348

Chain

903 – 1039

137

Integrin alpha-IIb light chain, form 2

PRO_0000016277

Regions

Topological domain

32 – 993

962

Extracellular Potential

Transmembrane

994 – 1019

26

Potential

Topological domain

1020 – 1039

20

Cytoplasmic Potential

Repeat

47 – 107

61

FG-GAP 1

Repeat

108 – ?

FG-GAP 2

Repeat

? – 262

FG-GAP 3

Repeat

263 – 316

54

FG-GAP 4

Repeat

317 – 384

68

FG-GAP 5

Repeat

385 – 444

60

FG-GAP 6

Repeat

445 – 497

53

FG-GAP 7

Calcium binding

274 – 282

9

Potential

Calcium binding

328 – 336

9

Potential

Calcium binding

396 – 404

9

Potential

Calcium binding

457 – 465

9

Potential

Motif

1022 – 1026

5

GFFKR motif

Amino acid modifications

Modified residue

891

1

Pyrrolidone carboxylic acid; in light chain form 1

Glycosylation

46

1

N-linked (GlcNAc...) Ref.16

Glycosylation

280

1

N-linked (GlcNAc...) Ref.16

Glycosylation

601

1

N-linked (GlcNAc...) Ref.16 Ref.21

Glycosylation

711

1

N-linked (GlcNAc...) Ref.16

Glycosylation

874

1

O-linked (GalNAc...); in alloantigen HPA-3B

Glycosylation

878

1

O-linked (GalNAc...) Ref.17

Glycosylation

962

1

N-linked (GlcNAc...)

Disulfide bond

87 ↔ 96

Ref.16

Disulfide bond

138 ↔ 161

Ref.16

Disulfide bond

177 ↔ 198

Ref.16

Disulfide bond

504 ↔ 515

Ref.16

Disulfide bond

521 ↔ 576

Ref.16

Disulfide bond

633 ↔ 639

Ref.16

Disulfide bond

705 ↔ 718

Ref.16

Disulfide bond

857 ↔ 911

Interchain (between heavy and light chains) Ref.16

Disulfide bond

916 ↔ 921

Ref.16

Natural variations

Alternative sequence

910 – 1039

130

SCDSA…DEEGE → VSRLSGLWPGLPGTHGAEGM GGGRGVRVCCGPLWATLGPW EHFK in isoform 3.

VSP_002736

Alternative sequence

948 – 981

34

Missing in isoform 2.

VSP_002737

Natural variant

40

1

T → I: dbSNP rs5915. Ref.34

VAR_014176

Natural variant

86

1

L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. Ref.39

VAR_030445

Natural variant

139

1

A → V in GT. Ref.40

VAR_030446

Natural variant

161

1

C → W in GT. Ref.38

VAR_030447

Natural variant

174

1

Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. Ref.42

VAR_030448

Natural variant

176

1

P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. Ref.37 Ref.40

VAR_009885

Natural variant

176

1

P → L in GT; impairs surface expression of alpha-IIb/beta-3. Ref.37

VAR_009886

Natural variant

202

1

F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. Ref.44

VAR_030449

Natural variant

207

1

T → I in GT. Ref.29

VAR_030450

Natural variant

214

1

L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. Ref.30

VAR_030451

Natural variant

222

1

F → L in GT. Ref.38

VAR_030452

Natural variant

267

1

G → E in GT. Ref.40

VAR_030453

Natural variant

273

1

G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. Ref.25

VAR_003979

Natural variant

313

1

G → A: dbSNP rs1126554. Ref.1 Ref.2

VAR_054820

Natural variant

320

1

F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. Ref.32

VAR_009887

Natural variant

329

1

V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. Ref.41

VAR_030454

Natural variant

355

1

E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. Ref.32 Ref.33

VAR_009888

Natural variant

358

1

R → H in GT; type II. Ref.27

VAR_003980

Natural variant

380

1

G → D in GT. Ref.40

VAR_030455

Natural variant

405

1

I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. Ref.40 Ref.41

VAR_030456

Natural variant

412

1

G → R in GT. Ref.38

VAR_030457

Natural variant

449

1

G → D in GT; type I. Ref.26

VAR_003981

Natural variant

456 – 457

2

Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.

VAR_030458

Natural variant

581

1

A → D in GT. Ref.40

VAR_030459

Natural variant

596

1

I → T in GT; type I. Ref.29 Ref.33

VAR_030460

Natural variant

649

1

V → L: dbSNP rs7207402.

VAR_054821

Natural variant

705

1

C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. Ref.35 Ref.40

VAR_030461

Natural variant

752

1

L → V in GT. Ref.40

VAR_030462

Natural variant

755

1

R → P in GT. Ref.40

VAR_030463

Natural variant

778

1

Q → P in GT; type II. Ref.31 Ref.32

VAR_003982

Natural variant

847

1

L → P in GT. Ref.38

VAR_030464

Natural variant

874

1

I → S Alloantigen HPA-3B. dbSNP rs5911. Ref.34

VAR_003983

Natural variant

943

1

P → L in GT; marked reduction in the rate of surface expression. Ref.45

VAR_030465

Natural variant

968

1

Y → N: dbSNP rs5914. Ref.34

VAR_014177

Natural variant

982

1

V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. Ref.43

VAR_030466

Natural variant

989

1

A → T

VAR_030467

Natural variant

1026

1

R → Q in GT. Ref.29

VAR_030468

Experimental info

Mutagenesis

1029 – 1030

2

PP → AA: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3. Ref.20

Sequence conflict

23

1

P → A in AAA35926. Ref.2

Sequence conflict

120

1

A → S in BAG37735. Ref.4

Sequence conflict

287 – 288

2

GA → VP in AAA53150. Ref.3

Sequence conflict

346

1

E → D in AAA35926. Ref.2

Sequence conflict

565

1

N → D in AAA35926. Ref.2

Sequence conflict

566

1

L → V in CAA29987. Ref.8

Sequence conflict

633

1

C → S in AAA60114. Ref.1

Sequence conflict

729

1

Q → E in CAA29987. Ref.8

Sequence conflict

971

1

P → A in AAA53150. Ref.3

Sequence conflict

1029

1

P → H in AAA35926. Ref.2

Sequence conflict

1029

1

P → H in AAA52588. Ref.10

Sequence conflict

1030

1

P → T in AAA52588. Ref.10

Secondary structure

1

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1039

Helix Strand Turn

Details...

Beta strand

36 – 38

3

Beta strand

40 – 43

4

Beta strand

52 – 58

7

Beta strand

64 – 69

6

Beta strand

78 – 80

3

Beta strand

84 – 88

5

Beta strand

107 – 110

4

Beta strand

113 – 118

6

Beta strand

126 – 131

6

Beta strand

134 – 139

6

Beta strand

143 – 148

6

Beta strand

159 – 164

6

Turn

166 – 168

3

Beta strand

171 – 174

4

Helix

183 – 188

6

Turn

189 – 193

5

Beta strand

202 – 206

5

Beta strand

210 – 216

7

Helix

219 – 222

4

Beta strand

225 – 230

6

Helix

231 – 237

7

Turn

259 – 263

5

Beta strand

268 – 273

6

Beta strand

283 – 288

6

Helix

291 – 294

4

Beta strand

297 – 302

6

Beta strand

307 – 312

6

Beta strand

324 – 327

4

Beta strand

330 – 333

4

Beta strand

336 – 341

6

Beta strand

345 – 348

4

Turn

349 – 351

3

Beta strand

352 – 355

4

Beta strand

358 – 362

5

Beta strand

366 – 368

3

Beta strand

375 – 379

5

Beta strand

391 – 393

3

Beta strand

400 – 402

3

Beta strand

405 – 409

5

Beta strand

419 – 423

5

Beta strand

435 – 439

5

Beta strand

450 – 456

7

Beta strand

461 – 463

3

Beta strand

465 – 470

6

Helix

471 – 473

3

Beta strand

475 – 479

5

Beta strand

1022 – 1024

3

Turn

1025 – 1027

3

Helix

1028 – 1031

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 14, 2009. Version 3. Checksum: 063EE298E026F116	FASTA	1,039	113,377
	10 20 30 40 50 60 MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS 70 80 90 100 110 120 HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA 130 140 150 160 170 180 RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN 190 200 210 220 230 240 TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP 250 260 270 280 290 300 GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI 310 320 330 340 350 360 LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY 370 380 390 400 410 420 LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV 430 440 450 460 470 480 LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR 490 500 510 520 530 540 AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ 550 560 570 580 590 600 LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL 610 620 630 640 650 660 NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN 670 680 690 700 710 720 VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL 730 740 750 760 770 780 GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE 790 800 810 820 830 840 LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP 850 860 870 880 890 900 SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP 910 920 930 940 950 960 SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL DQFVLQSHAW 970 980 990 1000 1010 1020 FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV LVGVLGGLLL LTILVLAMWK 1030 VGFFKRNRPP LEEDDEEGE
	Isoform 2. Checksum: 81C09F0D904CB534	FASTA	1,005	109,574
	10 20 30 40 50 60 MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS 70 80 90 100 110 120 HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA 130 140 150 160 170 180 RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN 190 200 210 220 230 240 TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP 250 260 270 280 290 300 GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI 310 320 330 340 350 360 LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY 370 380 390 400 410 420 LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV 430 440 450 460 470 480 LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR 490 500 510 520 530 540 AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ 550 560 570 580 590 600 LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL 610 620 630 640 650 660 NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN 670 680 690 700 710 720 VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL 730 740 750 760 770 780 GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE 790 800 810 820 830 840 LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP 850 860 870 880 890 900 SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP 910 920 930 940 950 960 SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQVWT QLLRALEERA 970 980 990 1000 IPIWWVLVGV LGGLLLLTIL VLAMWKVGFF KRNRPPLEED DEEGE
	Isoform 3. Checksum: 0100D4C5919320BE	FASTA	953	103,218
	10 20 30 40 50 60 MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS 70 80 90 100 110 120 HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA 130 140 150 160 170 180 RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN 190 200 210 220 230 240 TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP 250 260 270 280 290 300 GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI 310 320 330 340 350 360 LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY 370 380 390 400 410 420 LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV 430 440 450 460 470 480 LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR 490 500 510 520 530 540 AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ 550 560 570 580 590 600 LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL 610 620 630 640 650 660 NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN 670 680 690 700 710 720 VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL 730 740 750 760 770 780 GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE 790 800 810 820 830 840 LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP 850 860 870 880 890 900 SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP 910 920 930 940 950 SRLQDPVLVV SRLSGLWPGL PGTHGAEGMG GGRGVRVCCG PLWATLGPWE HFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors." Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., Schwartz E., Bennett J.S. J. Biol. Chem. 262:8476-8482(1987) [PubMed: 2439501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
[2]	"GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs." Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G. Mol. Biol. Rep. 14:27-33(1990) [PubMed: 2345548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
[3]	"Organization of the gene for platelet glycoprotein IIb." Heidenreich R., Eisman R., Surrey S., Delgrosso K., Bennett J.S., Schwartz E., Poncz M. Biochemistry 29:1232-1244(1990) [PubMed: 2322558] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Spleen.
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[7]	"Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs." Bray P.F., Leung C.S.-I., Shuman M.A. J. Biol. Chem. 265:9587-9590(1990) [PubMed: 2351656] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). Tissue: Erythroleukemia.
[8]	"cDNA clones for human platelet GPIIb corresponding to mRNA from megakaryocytes and HEL cells. Evidence for an extensive homology to other Arg-Gly-Asp adhesion receptors." Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E., Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G. Eur. J. Biochem. 171:87-93(1988) [PubMed: 3422188] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-1039 (ISOFORM 1).
[9]	"Platelet glycoprotein IIb. Chromosomal localization and tissue expression." Bray P.F., Rosa J.P., Johnston G.I., Shiu D.T., Cook R.G., Lau C., Kan Y.W., McEver R.P., Shuman M.A. J. Clin. Invest. 80:1812-1817(1987) [PubMed: 3479442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-1039 (ISOFORM 1).
[10]	"Isolation of the human platelet glycoprotein IIb gene and characterization of the 5' flanking region." Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G. Biochem. Biophys. Res. Commun. 156:595-601(1988) [PubMed: 2845986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62 AND 1021-1039.
[11]	"Platelet glycoproteins IIb and IIIa: evidence for a family of immunologically and structurally related glycoproteins in mammalian cells." Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S., Phillips D.R. Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986) [PubMed: 3534886] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-56 AND 903-917.
[12]	"Separation of important new platelet glycoproteins (GPIa, GPIc, GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies and gas-phase sequencing." Catimel B., Parmentier S., Leung L.L., McGregor J.L. Biochem. J. 279:419-425(1991) [PubMed: 1953640] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-42.
[13]	"Thermal stability of individual domains in platelet glycoprotein IIbIIIa." Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V. Eur. J. Biochem. 237:205-211(1996) [PubMed: 8620874] [Abstract] Cited for: PROTEIN SEQUENCE OF 32 AND 872.
[14]	"Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa." Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K. Blood 69:560-564(1987) [PubMed: 3801670] [Abstract] Cited for: PROTEIN SEQUENCE OF 487-501 AND 1026-1038.
[15]	"Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb. Localization of the epitopes for several monoclonal antibodies." Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A., Gonzalez-Rodriguez J. Biochem. J. 261:551-560(1989) [PubMed: 2476117] [Abstract] Cited for: PROTEIN SEQUENCE OF 903-922 AND 934-939.
[16]	"Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb." Calvete J.J., Henschen A., Gonzalez-Rodriguez J. Biochem. J. 261:561-568(1989) [PubMed: 2775232] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-46; ASN-280; ASN-601 AND ASN-711.
[17]	"Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression." Calvete J.J., Muniz-Diaz E. FEBS Lett. 328:30-34(1993) [PubMed: 7688323] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-878.
[18]	"Identification of a novel truncated alphaIIb integrin." Trikha M., Cai Y., Grignon D., Honn K.V. Cancer Res. 58:4771-4775(1998) [PubMed: 9809974] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[19]	"Characterization of the beta-chain N-terminus heterogeneity and the alpha-chain C-terminus of human platelet GPIIb. Posttranslational cleavage sites." Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J. FEBS Lett. 272:37-40(1990) [PubMed: 2226834] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE, PYROGLUTAMATE FORMATION AT GLN-891.
[20]	"Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations." Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C. J. Biol. Chem. 274:12945-12949(1999) [PubMed: 10212286] [Abstract] Cited for: MUTAGENESIS OF 1029-PRO-PRO-1030.
[21]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601, MASS SPECTROMETRY. Tissue: Plasma.
[22]	"RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3." Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., Treumann A., Moran N. Biochem. Biophys. Res. Commun. 369:1088-1093(2008) [PubMed: 18331836] [Abstract] Cited for: INTERACTION WITH RNF181.
[23]	"Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization." Bray P.F. Thromb. Haemost. 72:492-502(1994) [PubMed: 7878622] [Abstract] Cited for: REVIEW ON GT VARIANTS.
[24]	"Polymorphism of human platelet membrane glycoprotein IIb associated with the Baka/Bakb alloantigen system." Lyman S., Aster R.H., Visentin G.P., Newman P.J. Blood 75:2343-2348(1990) [PubMed: 2350579] [Abstract] Cited for: VARIANT HPA-3 (BAK).
[25]	"Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb." Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J., Parrella T., Fortina P., Bennett J.S. J. Clin. Invest. 93:172-179(1994) [PubMed: 8282784] [Abstract] Cited for: VARIANT GT ASP-273.
[26]	"A single amino acid substitution flanking the fourth calcium binding domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin complex." Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J. J. Biol. Chem. 269:4450-4457(1994) [PubMed: 7508443] [Abstract] Cited for: VARIANT GT ASP-449.
[27]	"Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association." Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J. J. Clin. Invest. 95:1553-1560(1995) [PubMed: 7706461] [Abstract] Cited for: VARIANT GT HIS-358.
[28]	"Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of alpha IIb: demonstration of the importance of calcium-binding domains in the conformation of alpha IIb beta 3." Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S., Poncz M. Blood 88:167-173(1996) [PubMed: 8704171] [Abstract] Cited for: VARIANT GT VAL-456-457-ASP DEL, CHARACTERIZATION OF VARIANT GT VAL-456-457-ASP DEL.
[29]	"Hematologically important mutations: Glanzmann thrombasthenia." French D.L., Coller B.S. Blood Cells Mol. Dis. 23:39-51(1997) [PubMed: 9215749] [Abstract] Cited for: VARIANTS GT ILE-207; THR-596 AND GLN-1026.
[30]	"Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa." Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L. Blood 91:1562-1571(1998) [PubMed: 9473221] [Abstract] Cited for: VARIANT GT PRO-214, CHARACTERIZATION OF VARIANT GT PRO-214.
[31]	"A Gln747-->Pro substitution in the IIb subunit is responsible for a moderate IIbbeta3 deficiency in Glanzmann thrombasthenia." Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M., Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y. Blood 92:2750-2758(1998) [PubMed: 9763559] [Abstract] Cited for: VARIANT GT PRO-778.
[32]	"Novel point mutations in the alphaIIb subunit (Phe289-->Ser, Glu324-->Lys and Gln747-->Pro) causing thrombasthenic phenotypes in four Japanese patients." Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y., Ikeda Y. Br. J. Haematol. 102:829-840(1998) [PubMed: 9722314] [Abstract] Cited for: VARIANTS GT SER-320; LYS-355 AND PRO-778.
[33]	"Double heterozygosity of the GPIIb gene in a Swiss patient with Glanzmann's thrombasthenia." Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K., Bourre F., Nurden A.T. Br. J. Haematol. 102:918-925(1998) [PubMed: 9734640] [Abstract] Cited for: VARIANTS GT LYS-355 AND THR-596.
[34]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANTS ILE-40; SER-874 AND ASN-968.
[35]	"Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes." Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R. Blood 93:866-875(1999) [PubMed: 9920835] [Abstract] Cited for: VARIANT GT ARG-705, CHARACTERIZATION OF VARIANT GT ARG-705.
[36]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[37]	"A naturally occurring mutation near the amino terminus of alphaIIb defines a new region involved in ligand binding to alphaIIbbeta3." Basani R.B., French D.L., Vilaire G., Brown D.L., Chen F., Coller B.S., Derrick J.M., Gartner T.K., Bennett J.S., Poncz M. Blood 95:180-188(2000) [PubMed: 10607701] [Abstract] Cited for: VARIANTS GT ALA-176 AND LEU-176.
[38]	"Description of 10 new mutations in platelet glycoprotein IIb (alphaIIb) and glycoprotein IIIa (beta3) genes." Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M., Negrier C. Platelets 12:486-495(2001) [PubMed: 11798398] [Abstract] Cited for: VARIANTS GT TRP-161; LEU-222; ARG-412 AND PRO-847.
[39]	"A Leu55 to Pro substitution in the integrin alphaIIb is responsible for a case of Glanzmann's thrombasthenia." Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S., Bourre F., Tani Y. Br. J. Haematol. 118:833-835(2002) [PubMed: 12181054] [Abstract] Cited for: VARIANT GT PRO-86, CHARACTERIZATION OF VARIANT GT PRO-86.
[40]	"Glanzmann's thrombasthenia: identification of 19 new mutations in 30 patients." D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M. Thromb. Haemost. 87:1034-1042(2002) [PubMed: 12083483] [Abstract] Cited for: VARIANTS GT VAL-139; ALA-176; GLU-267; ASP-380; THR-405; ASP-581; ARG-705; VAL-752 AND PRO-755.
[41]	"Two novel mutations in the alpha IIb calcium-binding domains identify hydrophobic regions essential for alpha IIbbeta 3 biogenesis." Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J., Coller B.S., French D.L. Blood 101:2268-2276(2003) [PubMed: 12424194] [Abstract] Cited for: VARIANTS GT PHE-329 AND THR-405, CHARACTERIZATION OF VARIANTS GT PHE-329 AND THR-405.
[42]	"A naturally occurring Tyr143His alpha IIb mutation abolishes alpha IIb beta 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: comparison with other mutations causing ligand-binding defects." Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H., Kosugi S., Kato H., Kurata Y., Matsuzawa Y. Blood 101:3485-3491(2003) [PubMed: 12506038] [Abstract] Cited for: VARIANT GT HIS-174, CHARACTERIZATION OF VARIANT GT HIS-174.
[43]	"Triple heterozygosity in the integrin alphaIIb subunit in a patient with Glanzmann's thrombasthenia." Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J., Blanchette V.S., Schmugge M., Rand M.L. J. Thromb. Haemost. 2:813-819(2004) [PubMed: 15099289] [Abstract] Cited for: VARIANT GT MET-982, CHARACTERIZATION OF VARIANT GT MET-982, VARIANT THR-989.
[44]	"A novel Phe171Cys mutation in integrin alpha causes Glanzmann thrombasthenia by abrogating alphaIIbbeta3 complex formation." Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U. J. Thromb. Haemost. 2:1167-1175(2004) [PubMed: 15219201] [Abstract] Cited for: VARIANT GT CYS-202, CHARACTERIZATION OF VARIANT GT CYS-202.
[45]	"Type II Glanzmann thrombasthenia in a compound heterozygote for the alpha IIb gene. A novel missense mutation in exon 27." Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C. Haematologica 91:1352-1359(2006) [PubMed: 17018384] [Abstract] Cited for: VARIANT GT LEU-943, CHARACTERIZATION OF VARIANT GT LEU-943.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.

IPI

IPI00218628.
IPI00218629.
IPI00295976.

PIR

A34269.

RefSeq

NP_000410.2.

UniGene

Hs.411312

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DPK	NMR	-	A	1020-1039	[»]
1DPQ	NMR	-	A	1020-1039	[»]
1JX5	model	-	A	32-483	[»]
1KUP	NMR	-	A	1018-1028	[»]
1KUZ	NMR	-	A	1018-1028	[»]
1M8O	NMR	-	A	1020-1039	[»]
1RN0	model	-	A	32-482	[»]
1S4W	NMR	-	A	1020-1039	[»]
1TYE	X-ray	2.90	A/C/E	32-483	[»]
1UV9	model	-	A	32-973	[»]
2K1A	NMR	-	A	989-1029	[»]
2K9J	NMR	-	A	989-1029	[»]
2KNC	NMR	-	A	991-1039	[»]
2VC2	X-ray	3.10	A	32-483	[»]
2VDK	X-ray	2.80	A	32-483	[»]
2VDL	X-ray	2.75	A	32-483	[»]
2VDM	X-ray	2.90	A	32-483	[»]
2VDN	X-ray	2.90	A	32-483	[»]
2VDO	X-ray	2.51	A	32-483	[»]
2VDP	X-ray	2.80	A	32-483	[»]
2VDQ	X-ray	2.59	A	32-483	[»]
2VDR	X-ray	2.40	A	32-483	[»]
3FCS	X-ray	2.55	A/C	32-989	[»]
3FCU	X-ray	2.90	A/C/E	32-488	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-68N.

IntAct

P08514. 2 interactions.

STRING

P08514.

PTM databases

PhosphoSite

P08514.

2-D gel databases

OGP

P08514.

Proteomic databases

PRIDE

P08514.

Genome annotation databases

Ensembl

ENST00000262407; ENSP00000262407; ENSG00000005961; Homo sapiens. [Genome view]

GeneID

3674.

KEGG

hsa:3674.

Organism-specific databases

CTD

3674.

GeneCards

GC17M039805.

H-InvDB

HIX0039058.

HGNC

HGNC:6138. ITGA2B.

HPA

CAB018611.

MIM

273800. phenotype.
607759. gene.

Orphanet

849. Glanzmann thrombasthenia.

PharmGKB

PA29938.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG402992.

HOVERGEN

P08514.

InParanoid

P08514.

OMA

IVACAPW.

OrthoDB

EOG9B2WGV.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6cyclingpathway. Arf6 signaling events.
ephrinbrevpathway. Ephrin B reverse signaling.
ptp1bpathway. Signaling events mediated by PTP1B.

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P08514.

Bgee

P08514.

CleanEx

HS_ITGA2B.

Genevestigator

P08514.

GermOnline

ENSG00000005961. Homo sapiens.

Family and domain databases

InterPro

IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR013513. Integrin_alpha_C.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]

Pfam

PF01839. FG-GAP. 3 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]

PRINTS

PR01185. INTEGRINA.

SMART

SM00191. Int_alpha. 5 hits.
[Graphical view]

PROSITE

PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00775. Tirofiban.

NextBio

14381.

SOURCE

Search...

Entry information

Entry name

ITA2B_HUMAN

Accession

Primary (citable) accession number: P08514
Secondary accession number(s): B2RCY8 , O95366, Q14443, Q17R67

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	April 14, 2009
Last modified:	December 15, 2009
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.